Thermodynamics of protein denaturation at high temperatures more than 100℃
Project/Area Number |
22570166
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Research Category |
Grant-in-Aid for Scientific Research (C)
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Allocation Type | Single-year Grants |
Section | 一般 |
Research Field |
Biophysics
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Research Institution | The Institute of Physical and Chemical Research |
Principal Investigator |
YUTANI Katsuhide 独立行政法人理化学研究所, タンパク質結晶構造解析研究グループ, 上級研究員 (90089889)
|
Co-Investigator(Renkei-kenkyūsha) |
MATSUURA Yoshinori 独立行政法人理化学研究所, タンパク質結晶構造解析研究グループ, リサーチアソシエイト (50513462)
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Project Period (FY) |
2010 – 2012
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Project Status |
Completed (Fiscal Year 2012)
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Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2012: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2011: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2010: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
|
Keywords | 蛋白質変性の熱力学 / 蛋白質の安定性 / 蛋白質熱変性の可逆性 / 示差走査熱量計 / 超好熱菌由来蛋白質 / 疎水性相互作用 / イオン相互作用 / CutA1 / DSC / 熱変性の可逆性 / 蛋白質の立体構造 / 蛋白質の熱変性 / 蛋白質の構造 / CutAl |
Research Abstract |
The heat-denaturation of proteins is usually irreversible at higher temperatures than around 70℃, because of aggregation after heat denaturation. Therefore, their thermodynamic characteristics are less well understood at the temperatures more than 70℃. In this study, we found that SH-free CutA1 mutant from E. coli and its hydrophobic mutants show very good reversibility of heat denaturation at pH 9. The denaturation temperatures of the hydrophobic mutants were 90-115℃. Then, we succeeded to experimentally obtain the thermodynamic parameters of protein denaturation over 100℃ by DSC.
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Report
(4 results)
Research Products
(27 results)
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[Journal Article] Structural characterization of a trapped folding intermediate of pyrrolidone carboxyl peptidase from a hyperthermophile2012
Author(s)
Mizuguchi, M., Takeuchi, M., Ohki, S., Nabeshima, Y., Kouno, T., Aizawa, T., Demura, M., Kawano, K., Yutani, K.
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Journal Title
Biochemistry
Volume: 51
Issue: 31
Pages: 6089-6096
DOI
Related Report
Peer Reviewed
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[Journal Article] A demetallation method for IMP-1 metallo-ss-lactamase with restored enzymatic activity upon addition of metal ion(s)2011
Author(s)
Yamaguchi Y, Ding S, Murakami E, Imamura K, Fuchigami S, Hashiguchi R, Yutani K, Mori H, Suzuki S, Arakawa Y, Kurosaki H
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Journal Title
ChemBioChem
Volume: 12
Issue: 13
Pages: 1979-1983
DOI
Related Report
Peer Reviewed
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